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The FEBS Journal, ISSN 1742-464X, 10/2017, Volume 284, Issue 19, pp. 3218 - 3229
.... 1H, 15N spectra showed that the C‐terminal SH3 domain of BIN1 isoform 1 (BIN1Iso1) is not mobile in solution but locked with the core of the protein... 
SH3 domain | nuclear magnetic resonance spectroscopy | protein–protein interaction | Tau | BIN1 | Alzheimer's disease | ALZHEIMERS-DISEASE | NMR-SPECTROSCOPY | BIOCHEMISTRY & MOLECULAR BIOLOGY | PATHOLOGY | MODEL | IDENTIFIES VARIANTS | AMPHIPHYSIN | MEMBRANE CURVATURE | protein-protein interaction | BINDING | EXPRESSION | GENOME-WIDE ASSOCIATION | Adaptor Proteins, Signal Transducing - chemistry | Humans | Peptides - genetics | tau Proteins - metabolism | tau Proteins - chemistry | Peptides - metabolism | Protein Isoforms - metabolism | tau Proteins - genetics | Protein Isoforms - chemistry | Tumor Suppressor Proteins - chemistry | Tumor Suppressor Proteins - genetics | Cloning, Molecular | Escherichia coli - metabolism | Nuclear Magnetic Resonance, Biomolecular | Neurons - metabolism | Protein Interaction Domains and Motifs | Nuclear Proteins - genetics | Binding Sites | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Gene Expression | Tumor Suppressor Proteins - metabolism | Neurons - chemistry | Peptides - chemistry | Models, Molecular | Recombinant Proteins - chemistry | Nuclear Proteins - metabolism | Recombinant Proteins - genetics | Nuclear Proteins - chemistry | Amino Acid Motifs | Sequence Homology, Amino Acid | Sequence Alignment | Protein Conformation, beta-Strand | Escherichia coli - genetics | Adaptor Proteins, Signal Transducing - genetics | Protein Binding | Kinetics | Adaptor Proteins, Signal Transducing - metabolism | Protein Isoforms - genetics | Nuclear magnetic resonance spectroscopy | Neurons | Protein-protein interactions | Spectroscopy | Clathrin | Nuclear magnetic resonance--NMR | Peptides | Neurodegenerative diseases | Pathogenesis | Complexity | Proteins | Magnetic resonance spectroscopy | Tau protein | Spectrum analysis | Isoforms | Alzheimers disease | Binding sites | tau Proteins/metabolism | Nuclear Proteins/chemistry | Protein Isoforms/chemistry | Protein Isoforms/genetics | Adaptor Proteins, Signal Transducing/genetics | Recombinant Proteins/metabolism | Peptides/metabolism | Life Sciences | Recombinant Proteins/chemistry | Adaptor Proteins, Signal Transducing/chemistry | Nuclear Proteins/metabolism | Tumor Suppressor Proteins/chemistry | Nuclear Proteins/genetics | Tumor Suppressor Proteins/metabolism | Protein Isoforms/metabolism | Peptides/chemistry | Recombinant Proteins/genetics | Biochemistry, Molecular Biology | Escherichia coli/genetics | Escherichia coli/metabolism | Adaptor Proteins, Signal Transducing/metabolism | Neurons/chemistry | Tumor Suppressor Proteins/genetics | tau Proteins/genetics | Neurons/metabolism | Peptides/genetics | tau Proteins/chemistry
Journal Article
The Plant cell, ISSN 1040-4651, 11/2012, Volume 24, Issue 11, pp. 4465 - 4482
.... Phenylpropanoid metabolism has to direct up to 30% of the carbon fixed by plants to the biosynthesis of lignin precursors... 
Proteins | Enzymes | Lignin | Protein metabolism | Sterols | RESEARCH ARTICLES | Hematocrit | Fluorescence | Cytochromes | Plants | Plant cells | ENDOPLASMIC-RETICULUM MEMBRANE | MOLECULAR-INTERACTIONS | ARABIDOPSIS-THALIANA | BIOCHEMISTRY & MOLECULAR BIOLOGY | CINNAMIC ACID | PHENYLALANINE AMMONIA-LYASE | CYTOCHROME P450 REDUCTASE | PLANT SCIENCES | CELL BIOLOGY | PHENYLPROPANOID PATHWAY | TANDEM AFFINITY PURIFICATION | ENZYME COMPLEXES | BINDING PROTEIN-1 | Green Fluorescent Proteins | Protein Multimerization | Cytochrome P-450 Enzyme System - metabolism | Endoplasmic Reticulum - metabolism | Trans-Cinnamate 4-Monooxygenase - genetics | Acyltransferases - metabolism | Recombinant Fusion Proteins | Coenzyme A Ligases - metabolism | Arabidopsis Proteins - metabolism | Trans-Cinnamate 4-Monooxygenase - metabolism | Lignin - metabolism | Plants, Genetically Modified | Membrane Proteins - metabolism | Transgenes | Acyl Coenzyme A - metabolism | Arabidopsis Proteins - genetics | Hydroxylation | Hydroxybenzoates - metabolism | Membrane Proteins - genetics | Tobacco - metabolism | Arabidopsis - metabolism | Protein Interaction Mapping | Arabidopsis - genetics | Plant Leaves - genetics | Plant Leaves - metabolism | Tobacco - genetics | Cytochrome P-450 Enzyme System - genetics | Phytochemistry | Physiological aspects | Biosynthesis | Research | Protein-protein interactions | Membrane proteins | Life Sciences | Molecular biology | Cellular Biology | Biochemistry, Molecular Biology
Journal Article
Molecular cell, ISSN 1097-2765, 2009, Volume 36, Issue 1, pp. 39 - 50
In the largest E3 ligase subfamily, Cul3 binds a BTB domain, and an associated protein-interaction domain such as MATH recruits substrates for ubiquitination... 
PROTEINS | ACTIVATION | PROTEIN | NRF2 | BIOCHEMISTRY & MOLECULAR BIOLOGY | SCF | ADAPTER | DEGRADATION | KEAP1 | DIMERIZATION | BTB DOMAIN | HEDGEHOG | CELL BIOLOGY | Transcription Factors - chemistry | Humans | Crystallography, X-Ray | Drosophila Proteins - metabolism | Mutation - physiology | Protein Multimerization - physiology | Protein Structure, Quaternary - physiology | Ubiquitination - physiology | Peptide Fragments - genetics | Repressor Proteins - metabolism | Amino Acid Sequence | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Repressor Proteins - genetics | Recombinant Fusion Proteins - chemistry | Nuclear Proteins - chemistry | Ubiquitin-Protein Ligases - chemistry | DNA-Binding Proteins - chemistry | Cullin Proteins - chemistry | Peptide Fragments - chemistry | Phosphoprotein Phosphatases - genetics | Consensus Sequence - physiology | Recombinant Fusion Proteins - genetics | Histones - metabolism | Ubiquitin-Protein Ligases - genetics | Drosophila melanogaster | Phosphoprotein Phosphatases - chemistry | Protein Binding - physiology | Adaptor Proteins, Signal Transducing - chemistry | Histones - chemistry | Protein Interaction Domains and Motifs - physiology | Phosphoprotein Phosphatases - metabolism | Recombinant Fusion Proteins - metabolism | DNA-Binding Proteins - metabolism | Cullin Proteins - metabolism | Nuclear Proteins - genetics | Peptide Fragments - metabolism | Repressor Proteins - chemistry | Nuclear Proteins - metabolism | Drosophila Proteins - chemistry | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Cullin Proteins - genetics | Transcription Factors - metabolism | Animals | Histones - genetics | Adaptor Proteins, Signal Transducing - genetics | Drosophila Proteins - genetics | Adaptor Proteins, Signal Transducing - metabolism | Ubiquitin | Chromatin | Phosphatases | Ligases | CHROMATIN | BASIC BIOLOGICAL SCIENCES | SUBSTRATES | FLEXIBILITY | GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE | LIGASES | DIMERS | PHOSPHATASES
Journal Article
eLife, ISSN 2050-084X, 2015, Volume 4, Issue 4, pp. 1 - 44
The AAA+ family ATPase TRIP13 is a key regulator of meiotic recombination and the spindle assembly checkpoint, acting on signaling proteins of the conserved HORMA domain family... 
N-Ethylmaleimide-Sensitive Proteins - metabolism | Mad2 Proteins - metabolism | Molecular Chaperones - metabolism | Caenorhabditis elegans Proteins - chemistry | Humans | Crystallography, X-Ray | Phylogeny | N-Ethylmaleimide-Sensitive Proteins - genetics | Amino Acid Sequence | Gene Expression | Caenorhabditis elegans - genetics | Cell Cycle Proteins - metabolism | Molecular Chaperones - genetics | Adenosine Triphosphatases - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Nuclear Proteins - chemistry | Caenorhabditis elegans - classification | Escherichia coli - genetics | Adenosine Triphosphatases - genetics | Escherichia coli Proteins - chemistry | Caenorhabditis elegans Proteins - genetics | Caenorhabditis elegans - enzymology | Adaptor Proteins, Signal Transducing - chemistry | Endopeptidase Clp - chemistry | M Phase Cell Cycle Checkpoints | Caenorhabditis elegans Proteins - metabolism | Molecular Sequence Data | Molecular Chaperones - chemistry | Cell Cycle Proteins - chemistry | Spindle Apparatus - genetics | Escherichia coli - metabolism | Cell Cycle Proteins - genetics | Carrier Proteins - chemistry | Nuclear Proteins - genetics | N-Ethylmaleimide-Sensitive Proteins - chemistry | Protein Structure, Tertiary | Recombinant Proteins - metabolism | ATPases Associated with Diverse Cellular Activities | Endopeptidase Clp - genetics | Escherichia coli Proteins - metabolism | Nuclear Proteins - metabolism | Endopeptidase Clp - metabolism | Mad2 Proteins - chemistry | Recombinant Proteins - genetics | Sequence Homology, Amino Acid | Carrier Proteins - genetics | Sequence Alignment | Animals | Carrier Proteins - metabolism | Adaptor Proteins, Signal Transducing - genetics | Mad2 Proteins - genetics | Escherichia coli Proteins - genetics | Protein Binding | Adenosine Triphosphatases - chemistry | Adaptor Proteins, Signal Transducing - metabolism | Spindle Apparatus - enzymology | Proteins | Medical research | Recombination | Software | Meiosis | Mammals | Chromosomes | DNA repair | Deoxyribonucleic acid--DNA | Adenosine triphosphatase | BASIC BIOLOGICAL SCIENCES
Journal Article
The Journal of biological chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 37, pp. 15287 - 15300
A remarkable property of the machinery for import of peroxisomal matrix proteins is that it can accept already folded proteins as substrates... 
CONSERVED CYSTEINE | HUMAN PTS1 RECEPTOR | DOCKING PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | CYCLING RECEPTOR | MACHINERY | MEMBRANE-PROTEIN | II SECRETION SYSTEM | AAA PEROXINS | TARGETING SIGNAL RECEPTOR | IMPORT RECEPTOR | Humans | Protein Multimerization | Mutation, Missense | Recombinant Fusion Proteins - metabolism | Biological Transport | Gene Deletion | Receptors, Cytoplasmic and Nuclear - chemistry | Membrane Proteins - metabolism | Protein Interaction Domains and Motifs | Peptide Fragments - genetics | Repressor Proteins - metabolism | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | Repressor Proteins - chemistry | Mutagenesis, Site-Directed | Membrane Proteins - genetics | Solubility | Recombinant Proteins - chemistry | Repressor Proteins - genetics | Receptors, Cytoplasmic and Nuclear - genetics | Recombinant Fusion Proteins - chemistry | Peroxisomes - metabolism | Amino Acid Motifs | Peptide Fragments - chemistry | Membrane Proteins - chemistry | Models, Biological | Peroxisome-Targeting Signal 1 Receptor | Endopeptidase K - metabolism | Mutation | Intracellular Membranes - metabolism | Amino Acid Substitution | Hydrogen-Ion Concentration | Receptors, Cytoplasmic and Nuclear - metabolism | ubiquitylation (ubiquitination) | docking | PEX5 | peroxisome | translocation module | protein import | protein sorting | receptor recycling | PEX14 | Cell Biology
Journal Article
Journal Article
Molecular cell, ISSN 1097-2765, 2019, Volume 74, Issue 6, pp. 1175 - 1188.e9
The condensin protein complex plays a key role in the structural organization of genomes... 
condensin | cohesin | SMC protein complex | ABC ATPase | genome organization | mitotic chromosome | structural biology | DNA loop extrusion | MOLECULAR-REPLACEMENT | FULLY-AUTOMATIC CHARACTERIZATION | STRUCTURE REFINEMENT | DATA-COLLECTION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | COHESIN RING | CHROMOSOME CONDENSATION | PROTEIN COMPLEXES | CRYSTALLOGRAPHY | DNA EXIT GATE | CELL BIOLOGY | Humans | Crystallography, X-Ray | Multiprotein Complexes - genetics | Saccharomyces cerevisiae - metabolism | Multiprotein Complexes - metabolism | Adenosine Triphosphate - metabolism | Binding Sites | Protein Subunits - genetics | Amino Acid Sequence | Gene Expression | Chromosomal Proteins, Non-Histone - metabolism | Adenosine Triphosphatases - metabolism | Models, Molecular | DNA - metabolism | Recombinant Fusion Proteins - chemistry | Saccharomyces cerevisiae Proteins - genetics | Nuclear Proteins - chemistry | DNA-Binding Proteins - chemistry | DNA - chemistry | Multiprotein Complexes - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Recombinant Fusion Proteins - genetics | Adenosine Triphosphatases - genetics | HeLa Cells | Saccharomyces cerevisiae Proteins - chemistry | Saccharomyces cerevisiae - genetics | Protein Multimerization | Recombinant Fusion Proteins - metabolism | Protein Subunits - metabolism | DNA-Binding Proteins - metabolism | Chromosomes - metabolism | Carrier Proteins - chemistry | Protein Interaction Domains and Motifs | Nuclear Proteins - genetics | Protein Conformation, alpha-Helical | Nuclear Proteins - metabolism | DNA-Binding Proteins - genetics | Chaetomium - genetics | Chromosomal Proteins, Non-Histone - genetics | DNA - genetics | Sequence Homology, Amino Acid | Carrier Proteins - genetics | Chaetomium - metabolism | Chromosomes - ultrastructure | Sequence Alignment | Carrier Proteins - metabolism | Protein Binding | Adenosine Triphosphatases - chemistry | Protein Subunits - chemistry | Adenosine Triphosphate - chemistry | Chromosomal Proteins, Non-Histone - chemistry | Proteins | Atoms | Genomics | Cells | Adenosine triphosphatase
Journal Article
Molecular cell, ISSN 1097-2765, 09/2010, Volume 39, Issue 6, pp. 963 - 974
... a critical role in tumorigenesis. However, the biochemical and cellular functions of this enigmatic family of proteins have remained elusive... 
NECDIN GENE | EMERGING ROLES | MELANOMA | KAP1 | CANCER/TESTIS ANTIGENS | BIOCHEMISTRY & MOLECULAR BIOLOGY | MDM2 INTERACTION | HOMOLOGOUS RECOMBINATION | CANCER-IMMUNOTHERAPY | CELL-LINES | EXPRESSION | CELL BIOLOGY | Melanoma-Specific Antigens - chemistry | Protein Interaction Domains and Motifs - physiology | Humans | Crystallography, X-Ray | Cytoplasm - metabolism | Intracellular Signaling Peptides and Proteins - metabolism | Neoplasm Proteins - metabolism | RING Finger Domains | Tripartite Motif-Containing Protein 28 | Ubiquitination | Cell Nucleus - metabolism | Transfection | Protein Structure, Quaternary | Antigens, Neoplasm - metabolism | Carrier Proteins - chemistry | Neoplasm Proteins - genetics | Intracellular Signaling Peptides and Proteins - genetics | Repressor Proteins - metabolism | Recombinant Proteins - metabolism | Antigens, Neoplasm - genetics | Cell Line | Biocatalysis | Tumor Suppressor Protein p53 - metabolism | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Repressor Proteins - genetics | Recombinant Proteins - genetics | Ubiquitin-Protein Ligases - chemistry | Carrier Proteins - genetics | Carrier Proteins - metabolism | Intracellular Signaling Peptides and Proteins - chemistry | Melanoma-Specific Antigens - metabolism | Cell Line, Tumor | Ubiquitin-Protein Ligases - genetics | Melanoma-Specific Antigens - genetics | Protein Binding - physiology | Ubiquitin | Antigens | Ligases | Crystals | Melanoma | Structure | Tumor proteins | Protein binding
Journal Article
The Journal of biological chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 40, pp. 15678 - 15690
Protein trafficking in the endosomal system involves the recognition of specific signals within the cytoplasmic domains (CDs... 
Humans | Virion - genetics | Adaptor Protein Complex 1 - chemistry | nef Gene Products, Human Immunodeficiency Virus - chemistry | Adaptor Protein Complex 2 - chemistry | Adaptor Protein Complex 1 - metabolism | Phosphatidylinositol 4,5-Diphosphate - metabolism | Human Immunodeficiency Virus Proteins - chemistry | Neoplasm Proteins - genetics | Binding Sites | Phosphatidylinositol 4,5-Diphosphate - chemistry | Protein Subunits - genetics | HIV-1 - metabolism | Gene Expression | Viral Regulatory and Accessory Proteins - genetics | Models, Molecular | Recombinant Proteins - chemistry | Neoplasm Proteins - chemistry | Adaptor Protein Complex 2 - genetics | Jurkat Cells - virology | Mammals | Phosphoserine - metabolism | Virion - metabolism | Viral Regulatory and Accessory Proteins - metabolism | nef Gene Products, Human Immunodeficiency Virus - genetics | Escherichia coli - genetics | Kinetics | Phosphoserine - chemistry | Viral Regulatory and Accessory Proteins - chemistry | Receptors, Cell Surface - genetics | Jurkat Cells - metabolism | Neoplasm Proteins - metabolism | Protein Subunits - metabolism | Adaptor Protein Complex 1 - genetics | Adaptor Protein Complex 2 - metabolism | Furin - genetics | Cloning, Molecular | Escherichia coli - metabolism | nef Gene Products, Human Immunodeficiency Virus - metabolism | Receptors, Cell Surface - chemistry | Protein Interaction Domains and Motifs | Furin - metabolism | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Furin - chemistry | Receptors, Cell Surface - metabolism | Recombinant Proteins - genetics | HIV-1 - genetics | Amino Acid Motifs | Human Immunodeficiency Virus Proteins - metabolism | Sequence Homology, Amino Acid | Sequence Alignment | Animals | Protein Conformation, beta-Strand | Protein Binding | Human Immunodeficiency Virus Proteins - genetics | Protein Subunits - chemistry | host-pathogen interaction | medium subunit | Serinc3 | human immunodeficiency virus (HIV) | clathrin | Membrane Biology | protein chemistry | protein complex | HIV-1 Vpu | acidic cluster | adaptor protein | kinetics | furin | phosphorylation | membrane trafficking | phosphoserine
Journal Article
Developmental cell, ISSN 1534-5807, 03/2010, Volume 18, Issue 3, pp. 397 - 409
.... The discovery that centromeric Rec8 is protected from separase during meiosis I by shugoshin/MEI-S332 proteins that bind PP2A phosphatase suggests that phosphorylation either of separase or cohesin... 
CELLBIO | RECOMBINATION | MAINTENANCE | KINETOCHORES | CENTROMERIC COHESION | HOMOLOGOUS CHROMOSOMES | REQUIRES | DEVELOPMENTAL BIOLOGY | SISTER-CHROMATID SEPARATION | PROTEIN PHOSPHATASE 2A | SEGREGATION | SHUGOSHIN | CELL BIOLOGY | Protein Kinases - metabolism | Casein Kinase Idelta - metabolism | Chromatin - metabolism | Meiosis - physiology | Phosphorylation | Protein Kinases - genetics | Casein Kinase I - genetics | Saccharomyces cerevisiae - genetics | Green Fluorescent Proteins - genetics | Centromere - metabolism | Recombinant Fusion Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Casein Kinase Iepsilon - metabolism | Cell Cycle Proteins - genetics | Genes, Fungal | Casein Kinase Iepsilon - genetics | Nuclear Proteins - genetics | Binding Sites | Casein Kinase Idelta - genetics | Protein-Serine-Threonine Kinases - metabolism | Endopeptidases - metabolism | Green Fluorescent Proteins - metabolism | Chromosomal Proteins, Non-Histone - metabolism | Separase | Cell Cycle Proteins - metabolism | Protein Phosphatase 2 - genetics | Protein-Serine-Threonine Kinases - genetics | Nuclear Proteins - metabolism | Saccharomyces cerevisiae Proteins - genetics | Chromosomal Proteins, Non-Histone - genetics | Saccharomyces cerevisiae - cytology | Meiosis - genetics | Endopeptidases - genetics | Models, Biological | Protein Phosphatase 2 - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Recombinant Fusion Proteins - genetics | Casein Kinase I - metabolism | Mutation | Chromosomal Proteins, Non-Histone - chemistry | Saccharomyces cerevisiae Proteins - chemistry | DNA replication | Phosphatases | Casein | Phosphotransferases | Protein binding
Journal Article